Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Mo‐nitrogenase"'
Publikováno v:
Microbial Cell Factories, Vol 20, Iss 1, Pp 1-14 (2021)
Abstract Background Biological nitrogen fixation is catalyzed by Mo-, V- and Fe-nitrogenases that are encoded by nif, vnf and anf genes, respectively. NifB is the key protein in synthesis of the cofactors of all nitrogenases. Most diazotrophic Paenib
Externí odkaz:
https://doaj.org/article/48f05f781f3e4e85bda3b5ab25596898
Publikováno v:
MicrobiologyOpen, Vol 9, Iss 6, Pp 1234-1246 (2020)
Abstract The photosynthetic α‐proteobacterium Rhodobacter capsulatus reduces and thereby fixes atmospheric dinitrogen (N2) by a molybdenum (Mo)‐nitrogenase and an iron‐only (Fe)‐nitrogenase. Differential expression of the structural genes of
Externí odkaz:
https://doaj.org/article/9a09ae5acb124683b6ddcc6e93856351
Publikováno v:
MicrobiologyOpen, Vol 8, Iss 12, Pp n/a-n/a (2019)
Abstract Rhodobacter capsulatus fixes atmospheric nitrogen (N2) by a molybdenum (Mo)‐nitrogenase and a Mo‐free iron (Fe)‐nitrogenase, whose production is induced or repressed by Mo, respectively. At low nanomolar Mo concentrations, both isoenzy
Externí odkaz:
https://doaj.org/article/b44bb51e29af4d85b4f1e5ebc5f2a853
Publikováno v:
Microbial Cell Factories, Vol 20, Iss 1, Pp 1-14 (2021)
Microbial Cell Factories
Microbial Cell Factories
Background Biological nitrogen fixation is catalyzed by Mo-, V- and Fe-nitrogenases that are encoded by nif, vnf and anf genes, respectively. NifB is the key protein in synthesis of the cofactors of all nitrogenases. Most diazotrophic Paenibacillus s
Publikováno v:
MicrobiologyOpen, Vol 9, Iss 6, Pp 1234-1246 (2020)
MicrobiologyOpen
MicrobiologyOpen
The photosynthetic α‐proteobacterium Rhodobacter capsulatus reduces and thereby fixes atmospheric dinitrogen (N2) by a molybdenum (Mo)‐nitrogenase and an iron‐only (Fe)‐nitrogenase. Differential expression of the structural genes of Mo‐nit
Autor:
Vichitphan, Kanit
The FeMo cofactor is one of two types of prosthetic group found in the larger of the two nitrogenase component proteins, called the MoFe protein, and it is strongly implicated as the substrate binding and reduction site. The glutamine-191 residue in
Externí odkaz:
http://hdl.handle.net/10919/11266
http://scholar.lib.vt.edu/theses/available/etd-12272001-160607
http://scholar.lib.vt.edu/theses/available/etd-12272001-160607
Autor:
Li, Hong
Mo-nitrogenase consists of two component proteins, the Fe protein and the MoFe protein. The site of substrate binding and reduction within the Mo-nitrogenase is provided by a metallocluster, the FeMo cofactor, located in the a-subunit of the MoFe pro
Externí odkaz:
http://hdl.handle.net/10919/27608
http://scholar.lib.vt.edu/theses/available/etd-05092002-213137/
http://scholar.lib.vt.edu/theses/available/etd-05092002-213137/
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Publikováno v:
MicrobiologyOpen, Vol 8, Iss 12, Pp n/a-n/a (2019)
MicrobiologyOpen
MicrobiologyOpen
Rhodobacter capsulatus fixes atmospheric nitrogen (N2) by a molybdenum (Mo)‐nitrogenase and a Mo‐free iron (Fe)‐nitrogenase, whose production is induced or repressed by Mo, respectively. At low nanomolar Mo concentrations, both isoenzymes are s
Akademický článek
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K zobrazení výsledku je třeba se přihlásit.
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